The Bcl2 family: regulators of the cellular life-or-death switch

By Suzanne Cory, Jerry M. Adams. Nature Reviews. Cancer, 2002

4,132 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/c92ce876d7443dfde7de8c165f687f82326f6c76

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Citations in the corpus

A guide to cell death pathways (2023, neutral): “BCL-2 is transcriptionally activated in human follicular lymphomas as a consequence of t(14;18) chromosomal translocation, and overexpression of anti-apoptotic BCL-2 family members is also found in many types of cancer cells 13 .”
Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy (2006, background): “Upon death receptor triggering, activation of caspase-8 may result in cleavage of Bid, a Bcl-2 family protein with a BH3 domain only, which in turn translocates to mitochondria to release cytochrome c thereby initiating a mitochondrial amplification loop (Cory and Adams, 2002).”
Apoptosis initiated by Bcl-2-regulated caspase activation independently of the cytochrome c/Apaf-1/caspase-9 apoptosome (2002, methodology): “b, Immortalized Apaf-1 pro-myeloid cells were cultured either untreated (2) or in the presence of 10 mg ml(21) etoposide (þ).”
The Bcl-2 family: roles in cell survival and oncogenesis (2003, background): “As the literature in this field is now vast, we also refer the reader to the relevant accompanying reviews and several other recent overviews (Gross et al., 1999a; Strasser et al., 2000; Cory and Adams, 2002; Borner, 2003; Adams, in press).”
Toxic proteins released from mitochondria in cell death (2004, background): “In most apoptotic conditions, the OMM becomes permeable, resulting in the leakage of cytochrome c into the cytosol by a process controlled by Bcl2 family members (Kluck et al., 1997; Yang et al., 1997; Cory and Adams, 2002).”
Recent advances in the development of protein–protein interactions modulators: mechanisms and clinical trials (2020, background): “Both antiapoptotic and pro-apoptotic members usually synergize in the form of dimers, having the role of apoptotic switch.(77,78) Proapoptotic proteins such as Bax and Bad have critical roles in the apoptosis.”
MicroRNA: Biogenesis, Function and Role in Cancer (2010, background): “The oncogenic BCL2 protein, commonly over expressed in various tumors and hematopoetic malignancies, promotes cell survival by evading apoptosis [264-266].”
Validating survivin as a cancer therapeutic target (2003, background): “The BCL2 family comprises molecules with pro- or anti-apoptotic function, which are identified by 1–4 copies of a BH (BCL2 homology) domain and a carboxy-terminal hydrophobic regio”
Pathways of apoptotic and non-apoptotic death in tumour cells (2004, background): “Cloning of the chromosome breakpoint of neoplastic B cells with the t(14;18) chromosome translocation.”
Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation. (2003, background): “The Bcl-2 family is composed of both pro-and antiapoptotic proteins that share sequence and structural homology (Cory and Adams 2002).”